Chromatographic Analysis of the N-Glycan Profile on Therapeutic Antibodies Using FcγRIIIa Affinity Column Chromatography.

ABSTRACT: N-Linked glycosylation on IgG has a profound impact on antibody functions. The relationship between the N-glycan structure and the binding affinity of FcγRIIIa, relating to antibody-dependent cell-mediated cytotoxicity (ADCC) activity, is important for the efficient development of a therapeutic antibody. Here, we report an influence of the N-glycan structure of IgGs, Fc fragments, and antibody-drug conjugates (ADCs) on FcγRIIIa affinity column chromatography. We compared the retention time of several IgGs with heterogeneous and homogeneous N-glycans. IgGs with a heterogeneous N-glycan structure provided several peaks in column chromatography. On the other hand, homogeneous IgGs and ADCs gave a single peak in column chromatography. The length of glycan on

SUBMITTER: Hiranyakorn M 

PROVIDER: S-EPMC10173337 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature